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Information on EC 4.2.1.33 - 3-isopropylmalate dehydratase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LYT7

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.33 3-isopropylmalate dehydratase
IUBMB Comments
Forms part of the leucine biosynthesis pathway. The enzyme brings about the interconversion of the two isomers of isopropylmalate. It contains an iron-sulfur cluster.
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9LYT7
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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Synonyms
isopropylmalate isomerase, leucd, alpha-isopropylmalate isomerase, ipmi ssu1, isopropylmalate dehydratase, 3-isopropylmalate dehydratase, ipm isomerase, mj0499, alpha-ipm isomerase, leu1s, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isopropylmalate isomerase
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Alpha-IPM isomerase
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-
-
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alpha-isopropylmalate isomerase
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-
-
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beta-Isopropylmalate dehydratase
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-
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dehydratase,beta-isopropylmalate
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-
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IPM dehydratase
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-
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IPMI SSU1
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isopropylmalate isomerase small subunit1
isopropylmalate dehydratase
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isopropylmalate isomerase
SOI10
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-
-
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Superoxide-inducible protein 10
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
(2R,3S)-3-isopropylmalate hydro-lyase (2-isopropylmaleate-forming)
Forms part of the leucine biosynthesis pathway. The enzyme brings about the interconversion of the two isomers of isopropylmalate. It contains an iron-sulfur cluster.
CAS REGISTRY NUMBER
COMMENTARY hide
37290-72-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R,3S)-3-isopropylmalate
2-isopropylmaleate + H2O
show the reaction diagram
-
-
-
-
?
(2S)-2-isopropylmalate
(2R,3S)-3-isopropylmalate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2R,3S)-3-isopropylmalate
2-isopropylmaleate + H2O
show the reaction diagram
-
-
-
-
?
(2S)-2-isopropylmalate
(2R,3S)-3-isopropylmalate
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
small subunit
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
expression in all floral tissues including sepal, stamen, pistil as well as pollen grains, but it is only present at both ends of developing siliques
Manually annotated by BRENDA team
additional information
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semi-quantitative RT-PCR analysis of temporal and spatial expression of AtLeuC and AtLeuD genes, overview. The tissue-specifis expression analysis reveals that the patterns of small subunits AtLeuD1 and AtLeuD2 expression are similar, but distinct from that of AtLeuD3
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
presence of different heterodimeric IPMIs in chloroplasts with distinct substrate specificities for Leu or glucosinolate metabolism
Manually annotated by BRENDA team
additional information
-
analysis of subcellular localization of AtLeuC and AtLeuDs within Arabidopsis chloroplast compartments, overview
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
homozygous ipmi 3-1mutants can be established. In leaves and seeds of the ipmi ssu3-1 mutant few significant changes in amino acid content. Met levels are unchanged in ipmi ssu3-1 and S-methylmethionine can not be detected
malfunction
metabolism
physiological function
additional information
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physical interaction between isopropylmalate isomerase (IPMI) and isopropylmalate dehydrogenases (IPMDHs) in planta. The complex formation may represent a new regulatory mechanism controlling Met chain-elongation and/or Leu biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LEUD2_ARATH
253
0
27208
Swiss-Prot
Chloroplast (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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construction of AtLeuD1 T-DNA knockout mutant and AtLeuD -RNAi plants, i.e. specific AtLeuD2 -RNAi, AtLeuD -RNAi, atleud1 /AtLeuD2 -RNAi and atleud1 /AtLeuD -RNAi. Lethal phenotype of the atleud3 mutant
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of FLAG-tagged LeuC and of the three LeuD isoforms in transgenic Arabidosis thaliana plants, interaction analysis, overview
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full length reading frame of IPMI small subunit 2 fused in frame to the 5' end of the gene encoding the green fluorescent protein in the vector psmGFP4. Construct transiently expressed in tobacco protoplasts and stably transformed into Arabidopsis plants
recombinant expression of GFP-tagged large and small subunit 1 in Arabidopsis thaliana leaves
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in ipmi ssu3-1 plants, absence of mature mRNAs in homozygous plants and the knockout of these genes by T-DNAs
in ipmi ssu2-1 plants, absence of mature mRNAs in homozygous plants and the knockout of these genes by T-DNAs
in the ipmilsu1-2mutant mRNA levels are reduced to 65 and 50% of the wild-type standard in seedlings and rosette leaves, respectively, while IPMI large subunit 1 transcript levels are reduced to 40 and 27% of wild-type in these tissues of ipmi lsu1-1 plants. Strongest reduction in ipmi lsu1-3 seedlings (21% of wild-type), while the IPMI large subunit 1 mRNA level in ipmi lsu1-3 reaches about 29% of the wild-type level in leaves
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Knill, T.; Reichelt, M.; Paetz, C.; Gershenzon, J.; Binder, S.
Arabidopsis thaliana encodes a bacterial-type heterodimeric isopropylmalate isomerase involved in both Leu biosynthesis and the Met chain elongation pathway of glucosinolate formation
Plant Mol. Biol.
71
227-239
2009
Arabidopsis thaliana (Q94AR8), Arabidopsis thaliana (Q94AR8 AND Q9ZW84), Arabidopsis thaliana (Q9LYT7), Arabidopsis thaliana (Q9ZW84), Arabidopsis thaliana (Q9ZW85), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q94AR8 AND Q9ZW84)
Manually annotated by BRENDA team
He, Y.; Chen, B.; Pang, Q.; Strul, J.M.; Chen, S.
Functional specification of Arabidopsis isopropylmalate isomerases in glucosinolate and leucine biosynthesis
Plant Cell Physiol.
51
1480-1487
2010
Arabidopsis thaliana
Manually annotated by BRENDA team
Imhof, J.; Huber, F.; Reichelt, M.; Gershenzon, J.; Wiegreffe, C.; Laechler, K.; Binder, S.
The small subunit 1 of the Arabidopsis isopropylmalate isomerase is required for normal growth and development and the early stages of glucosinolate formation
PLoS ONE
9
e91071
2014
Arabidopsis thaliana
Manually annotated by BRENDA team
Chen, L.Q.; Chhajed, S.; Zhang, T.; Collins, J.M.; Pang, Q.; Song, W.; He, Y.; Chen, S.
Protein complex formation in methionine chain-elongation and leucine biosynthesis
Sci. Rep.
11
3524
2021
Arabidopsis thaliana, Arabidopsis thaliana Col0
Manually annotated by BRENDA team